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Potassium voltage-gated channel subfamily C member 2 (Potassium channel voltage-gated Shaw-related subfamily C member 2) (Shaw-like potassium channel) (Voltage-gated potassium channel subunit Kv3.2)

 KCNC2_RAT               Reviewed;         638 AA.
P22462; P22461; P22463; Q63735;
01-AUG-1991, integrated into UniProtKB/Swiss-Prot.
01-AUG-1991, sequence version 1.
23-MAY-2018, entry version 157.
RecName: Full=Potassium voltage-gated channel subfamily C member 2 {ECO:0000312|RGD:628829};
AltName: Full=Potassium channel voltage-gated Shaw-related subfamily C member 2 {ECO:0000312|RGD:628829};
AltName: Full=Shaw-like potassium channel {ECO:0000303|PubMed:1879548};
AltName: Full=Voltage-gated potassium channel subunit Kv3.2 {ECO:0000303|PubMed:1879548};
Name=Kcnc2 {ECO:0000312|RGD:628829};
Rattus norvegicus (Rat).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Rattus.
NCBI_TaxID=10116;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, BIOPHYSICOCHEMICAL
PROPERTIES, ENZYME REGULATION, AND SUBCELLULAR LOCATION.
TISSUE=Brain;
PubMed=2367536; DOI=10.1073/pnas.87.13.5227;
McCormack T., de Miera E.C.V.-S., Rudy B.;
"Molecular cloning of a member of a third class of Shaker-family K+
channel genes in mammals.";
Proc. Natl. Acad. Sci. U.S.A. 87:5227-5231(1990).
[2]
SEQUENCE REVISION.
PubMed=2023956; DOI=10.1073/pnas.88.9.4060-b;
McCormack T., de Miera E.C.V.-S., Rudy B.;
"Molecular cloning of a member of a third class of Shaker-family K+
channel genes in mammals.";
Proc. Natl. Acad. Sci. U.S.A. 88:4060-4060(1991).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION,
BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
TISSUE=Brain;
PubMed=1879548; DOI=10.1016/0014-5793(91)81026-5;
Luneau C.J., Wiedmann R., Smith J.S., Williams J.B.;
"Shaw-like rat brain potassium channel cDNA's with divergent 3'
ends.";
FEBS Lett. 288:163-167(1991).
[4]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 4).
PubMed=1378392;
Rettig J., Wunder F., Stocker M., Lichtinghagen R., Mastiaux F.,
Beckh S., Kues W., Pedarzani P., Schroeter K.H., Ruppersberg J.P.,
Veh R., Pongs O.;
"Characterization of a Shaw-related potassium channel family in rat
brain.";
EMBO J. 11:2473-2486(1992).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY.
PubMed=1374908; DOI=10.1073/pnas.89.10.4603;
Baker H., Pollock J., Ellisman M., Kentros C., Miera E., Serodio P.,
Weiser M., Rudy B., Fruhling D.;
"Region-specific expression of a K+ channel gene in brain.";
Proc. Natl. Acad. Sci. U.S.A. 89:4603-4607(1992).
[6]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
TISSUE SPECIFICITY.
PubMed=8120636;
Weiser M., Vega-Saenz de Miera E., Kentros C., Moreno H., Franzen L.,
Hillman D., Baker H., Rudy B.;
"Differential expression of Shaw-related K+ channels in the rat
central nervous system.";
J. Neurosci. 14:949-972(1994).
[7]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION,
PHOSPHORYLATION, MUTAGENESIS OF SER-563 AND SER-564, SUBCELLULAR
LOCATION, AND TISSUE SPECIFICITY.
PubMed=7643197;
Moreno H., Kentros C., Bueno E., Weiser M., Hernandez A.,
Vega-Saenz de Miera E., Ponce A., Thornhill W., Rudy B.;
"Thalamocortical projections have a K+ channel that is phosphorylated
and modulated by cAMP-dependent protein kinase.";
J. Neurosci. 15:5486-5501(1995).
[8]
SUBCELLULAR LOCATION (ISOFORMS 1; 2 AND 3).
PubMed=9307441; DOI=10.1007/s002329900278;
Ponce A., Vega-Saenz de Miera E., Kentros C., Moreno H., Thornhill B.,
Rudy B.;
"K+ channel subunit isoforms with divergent carboxy-terminal sequences
carry distinct membrane targeting signals.";
J. Membr. Biol. 159:149-159(1997).
[9]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME REGULATION, SUBUNIT,
INTERACTION WITH KCNC1, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10482766;
Hernandez-Pineda R., Chow A., Amarillo Y., Moreno H., Saganich M.,
Vega-Saenz de Miera E.C., Hernandez-Cruz A., Rudy B.;
"Kv3.1-Kv3.2 channels underlie a high-voltage-activating component of
the delayed rectifier K+ current in projecting neurons from the globus
pallidus.";
J. Neurophysiol. 82:1512-1528(1999).
[10]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=10414968;
Baranauskas G., Tkatch T., Surmeier D.J.;
"Delayed rectifier currents in rat globus pallidus neurons are
attributable to Kv2.1 and Kv3.1/3.2 K(+) channels.";
J. Neurosci. 19:6394-6404(1999).
[11]
REVIEW.
PubMed=10414303; DOI=10.1111/j.1749-6632.1999.tb11295.x;
Rudy B., Chow A., Lau D., Amarillo Y., Ozaita A., Saganich M.,
Moreno H., Nadal M.S., Hernandez-Pineda R., Hernandez-Cruz A.,
Erisir A., Leonard C., Vega-Saenz de Miera E.;
"Contributions of Kv3 channels to neuronal excitability.";
Ann. N. Y. Acad. Sci. 868:304-343(1999).
[12]
REVIEW.
PubMed=11506885; DOI=10.1016/S0166-2236(00)01892-0;
Rudy B., McBain C.J.;
"Kv3 channels: voltage-gated K+ channels designed for high-frequency
repetitive firing.";
Trends Neurosci. 24:517-526(2001).
[13]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION, AND
MUTAGENESIS OF SER-563 AND SER-564.
PubMed=11281123; DOI=10.1111/j.1469-7793.2001.0345k.x;
Moreno H., Vega-Saenz de Miera E., Nadal M.S., Amarillo Y., Rudy B.;
"Modulation of Kv3 potassium channels expressed in CHO cells by a
nitric oxide-activated phosphatase.";
J. Physiol. (Lond.) 530:345-358(2001).
[14]
FUNCTION, BIOPHYSICOCHEMICAL PROPERTIES, SUBUNIT, INTERACTION WITH
KCNC1; KCNE1; KCNE2 AND KCNE3, AND SUBCELLULAR LOCATION.
PubMed=14679187; DOI=10.1074/jbc.M310501200;
Lewis A., McCrossan Z.A., Abbott G.W.;
"MinK, MiRP1, and MiRP2 diversify Kv3.1 and Kv3.2 potassium channel
gating.";
J. Biol. Chem. 279:7884-7892(2004).
[15]
TISSUE SPECIFICITY.
PubMed=16413129; DOI=10.1016/j.neuroscience.2005.11.047;
McDonald A.J., Mascagni F.;
"Differential expression of Kv3.1b and Kv3.2 potassium channel
subunits in interneurons of the basolateral amygdala.";
Neuroscience 138:537-547(2006).
[16]
INDUCTION.
PubMed=18775767; DOI=10.1016/j.neuroscience.2008.08.008;
Grabert J., Wahle P.;
"Neuronal activity and TrkB ligands influence Kv3.1b and Kv3.2
expression in developing cortical interneurons.";
Neuroscience 156:618-629(2008).
[17]
TISSUE SPECIFICITY, AND INDUCTION.
PubMed=18708127; DOI=10.1016/j.neuroscience.2008.07.035;
Grabert J., Wahle P.;
"Visual experience regulates Kv3.1b and Kv3.2 expression in developing
rat visual cortex.";
Neuroscience 158:654-664(2009).
[18]
FUNCTION, SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
PubMed=22831914; DOI=10.1016/j.ceca.2012.06.007;
Kuznetsov K.I., Grygorov O.O., Maslov V.Y., Veselovsky N.S.,
Fedulova S.A.;
"Kv3 channels modulate calcium signals induced by fast firing patterns
in the rat retinal ganglion cells.";
Cell Calcium 52:405-411(2012).
-!- FUNCTION: Voltage-gated potassium channel that mediates
transmembrane potassium transport in excitable membranes,
primarily in the brain. Contributes to the regulation of the fast
action potential repolarization and in sustained high-frequency
firing in neurons of the central nervous system (PubMed:10482766,
PubMed:10414968, PubMed:11506885, PubMed:22831914). Homotetramer
channels mediate delayed-rectifier voltage-dependent potassium
currents that activate rapidly at high-threshold voltages and
inactivate slowly (PubMed:2367536, PubMed:1879548, PubMed:8120636,
PubMed:7643197, PubMed:10414303). Forms tetrameric channels
through which potassium ions pass in accordance with their
electrochemical gradient. The channel alternates between opened
and closed conformations in response to the voltage difference
across the membrane (PubMed:2367536, PubMed:1879548,
PubMed:8120636, PubMed:7643197). Can form functional
homotetrameric channels and heterotetrameric channels that contain
variable proportions of KCNC1, and possibly other family members
as well; channel properties depend on the type of alpha subunits
that are part of the channel (PubMed:10482766, PubMed:14679187).
Channel properties may be modulated either by the association with
ancillary subunits, such as KCNE1, KCNE2 and KCNE3 or indirectly
by nitric oxide (NO) through a cGMP- and PKG-mediated signaling
cascade, slowing channel activation and deactivation of delayed
rectifier potassium channels (PubMed:11281123, PubMed:14679187).
Contributes to fire sustained trains of very brief action
potentials at high frequency in retinal ganglion cells,
thalamocortical and suprachiasmatic nucleus (SCN) neurons and in
hippocampal and neocortical interneurons (PubMed:10482766,
PubMed:10414968, PubMed:11506885, PubMed:22831914). Sustained
maximal action potential firing frequency in inhibitory
hippocampal interneurons is negatively modulated by histamine H2
receptor activation in a cAMP- and protein kinase (PKA)
phosphorylation-dependent manner. Plays a role in maintaining the
fidelity of synaptic transmission in neocortical GABAergic
interneurons by generating action potential (AP) repolarization at
nerve terminals, thus reducing spike-evoked calcium influx and
GABA neurotransmitter release. Required for long-range
synchronization of gamma oscillations over distance in the
neocortex. Contributes to the modulation of the circadian rhythm
of spontaneous action potential firing in suprachiasmatic nucleus
(SCN) neurons in a light-dependent manner (By similarity).
{ECO:0000250|UniProtKB:Q14B80, ECO:0000269|PubMed:10414968,
ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:11281123,
ECO:0000269|PubMed:11506885, ECO:0000269|PubMed:14679187,
ECO:0000269|PubMed:1879548, ECO:0000269|PubMed:22831914,
ECO:0000269|PubMed:2367536, ECO:0000269|PubMed:7643197,
ECO:0000269|PubMed:8120636, ECO:0000305|PubMed:10414303,
ECO:0000305|PubMed:11506885}.
-!- ENZYME REGULATION: Inhibited by Stichodactyla helianthus peptide
ShK (By similarity). Inhibited by millimolar levels of
tetraethylammonium (TEA). Contrary to other channels, inhibited
only by millimolar levels of 4-aminopyridine (4-AP)
(PubMed:2367536, PubMed:1879548, PubMed:7643197, PubMed:10482766,
PubMed:10414303). {ECO:0000250|UniProtKB:Q96PR1,
ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:1879548,
ECO:0000269|PubMed:2367536, ECO:0000269|PubMed:7643197,
ECO:0000305|PubMed:10414303}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
Note=Homotetrameric channels expressed in xenopus oocytes or in
mammalian non-neuronal cells display delayed-rectifier voltage-
dependent potassium currents, that are rapidly activated during
membrane depolarization, i.e within a risetime of a few msec.
After that, inactivates very slowly, i.e within about >800 msec.
Their activation requires a threshold potential at about -10 mV,
with a midpoint activation at about 12.1 mV and a steepness
parameter of about 8.4 mV (PubMed:2367536, PubMed:1879548,
PubMed:8120636, PubMed:7643197, PubMed:10414303,
PubMed:11281123, PubMed:14679187). The voltage-dependence of
activation and inactivation and other channel characteristics
vary depending on the experimental conditions, the expression
system, the presence or absence of ancillary subunits and post-
translational modifications (PubMed:7643197, PubMed:10414303,
PubMed:11281123, PubMed:14679187). {ECO:0000269|PubMed:11281123,
ECO:0000269|PubMed:14679187, ECO:0000269|PubMed:1879548,
ECO:0000269|PubMed:2367536, ECO:0000269|PubMed:7643197,
ECO:0000269|PubMed:8120636, ECO:0000305|PubMed:10414303};
-!- SUBUNIT: Homotetramer and heterotetramer with other channel-
forming alpha subunits, such as KCNC1. Interacts with KCNC1
(PubMed:10482766, PubMed:14679187). Homotetramer or heterotetramer
channel activity is regulated by association with modulating
ancillary subunits such as KCNE1, KCNE2 and KCNE3, creating a
functionally diverse range of channel complexes. Interacts with
KCNE1, KCNE2 and KCNE3 (PubMed:14679187).
{ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:14679187}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10414968,
ECO:0000269|PubMed:10482766, ECO:0000269|PubMed:14679187,
ECO:0000269|PubMed:1879548, ECO:0000269|PubMed:22831914,
ECO:0000269|PubMed:2367536, ECO:0000269|PubMed:7643197,
ECO:0000269|PubMed:8120636}; Multi-pass membrane protein
{ECO:0000255}. Membrane {ECO:0000269|PubMed:11281123}; Multi-pass
membrane protein {ECO:0000255}. Perikaryon
{ECO:0000269|PubMed:10482766}. Cell projection, axon
{ECO:0000269|PubMed:7643197}. Cell junction, synapse
{ECO:0000269|PubMed:7643197}. Cell junction, synapse, synaptosome
{ECO:0000269|PubMed:7643197}. Cell projection, dendrite
{ECO:0000250|UniProtKB:Q14B80}. Cell junction, synapse,
postsynaptic cell membrane {ECO:0000250|UniProtKB:Q14B80}. Cell
junction, synapse, presynaptic cell membrane
{ECO:0000250|UniProtKB:Q14B80}. Note=Localizes on the surface of
cell somata, proximal dendrites and axonal membranes. Also
detected throughout the neuropil. Localized in starburst cell
somata and proximal dendrite processes. Colocalized with GABA in
presynaptic terminals. Clustered in patches in somatic and
proximal dendritic membrane as well as in axons and presnypatic
terminals of GABAergic interneurons; some of these patches are
found near postsynaptic sites (By similarity). Colocalizes with
parvalbumin in globus pallidus neurons (PubMed:10482766).
Localizes in thalamocortical axons and synapses (PubMed:7643197).
{ECO:0000250|UniProtKB:Q14B80, ECO:0000269|PubMed:10482766,
ECO:0000269|PubMed:7643197}.
-!- SUBCELLULAR LOCATION: Isoform 1: Apical cell membrane
{ECO:0000269|PubMed:9307441}.
-!- SUBCELLULAR LOCATION: Isoform 2: Apical cell membrane
{ECO:0000269|PubMed:9307441}.
-!- SUBCELLULAR LOCATION: Isoform 3: Basolateral cell membrane
{ECO:0000269|PubMed:9307441}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1; Synonyms=KV3.2B {ECO:0000303|PubMed:1879548};
IsoId=P22462-1; Sequence=Displayed;
Name=2; Synonyms=KV3.2C {ECO:0000303|PubMed:1879548};
IsoId=P22462-2; Sequence=VSP_001018;
Name=3; Synonyms=KV3.2A, KShIIIA.1 {ECO:0000303|PubMed:2367536};
IsoId=P22462-3; Sequence=VSP_001019;
Name=4;
IsoId=P22462-4; Sequence=VSP_001020;
-!- TISSUE SPECIFICITY: Expressed in neurons of the visual cortex
during postnatal development (PubMed:18708127). Expressed in
neurons of the globus pallidus at postnatal age day 7 (P7), onward
(PubMed:10482766). Expressed in thalamic relay neurons. Expressed
in neurons in layer IV and deeper cortical layers of the
neocortex. Expressed in hippocampal interneurons (PubMed:7643197).
Expressed in nonpyramidal interneurons in the basolateral amygdala
(PubMed:16413129). Expressed in retinal ganglion cells (at protein
level) (PubMed:22831914). Widely expressed in the brain
(PubMed:1879548, PubMed:8120636). Expressed in numerous thalamic
relay neurons throughout the dorsal thalamus. Expressed in
interneurons of the deep layers V-VI of the cerebral cortex, the
CA1 and CA3 pyramidal and dentate gyrus (DG) granule cells of the
hippocampus, in neurons of the caudate-putamen, globus pallidus
and subthalamic nucleus. Also expressed in the optic layer of
interior colliculus, the inferior colliculus, the red nucleus, the
medial geniculate, the ventral lateral lemiscus, the
reticulotegmental nucleus and in the deep cerebellar nuclei
(PubMed:1374908, PubMed:8120636, PubMed:7643197, PubMed:18708127).
Expressed in globus pallidus (GP) neurons (PubMed:10414968).
{ECO:0000269|PubMed:10414968, ECO:0000269|PubMed:10482766,
ECO:0000269|PubMed:1374908, ECO:0000269|PubMed:16413129,
ECO:0000269|PubMed:18708127, ECO:0000269|PubMed:1879548,
ECO:0000269|PubMed:22831914, ECO:0000269|PubMed:7643197,
ECO:0000269|PubMed:8120636}.
-!- INDUCTION: Up-regulated in visual cortex during the second
postnatal week from dark-reared animals (at protein level). Down-
regulated in visual cortex by active visual experience until
postnatal day P40 of dark-reared animals (PubMed:18708127). Down-
regulated by chronic action potential activity deprivation in
organotypic culture of the visual cortex (PubMed:18775767).
{ECO:0000269|PubMed:18708127, ECO:0000269|PubMed:18775767}.
-!- DOMAIN: The transmembrane segment S4 functions as voltage-sensor
and is characterized by a series of positively charged amino acids
at every third position. Channel opening and closing is effected
by a conformation change that affects the position and orientation
of the voltage-sensor paddle formed by S3 and S4 within the
membrane. A transmembrane electric field that is positive inside
would push the positively charged S4 segment outwards, thereby
opening the pore, while a field that is negative inside would pull
the S4 segment inwards and close the pore. Changes in the position
and orientation of S4 are then transmitted to the activation gate
formed by the inner helix bundle via the S4-S5 linker region.
{ECO:0000250|UniProtKB:P63142}.
-!- PTM: Phosphorylated by PKA in cortical synaptosomes
(PubMed:7643197). cAMP-dependent phosphorylation inhibits channel
activity (PubMed:7643197). Histamine H2 receptor- and PKA-induced
phosphorylation extends action potential spike duration, reduces
action potential spike amplitude, sustains maximum firing
frequency in hippocampal interneurons; also reduces the incidence
of high-frequency oscillations in hippocampal CA3 pyramidal cell
layers (By similarity). {ECO:0000250|UniProtKB:P63142,
ECO:0000269|PubMed:7643197}.
-!- SIMILARITY: Belongs to the potassium channel family. C (Shaw) (TC
1.A.1.2) subfamily. Kv3.2/KCNC2 sub-subfamily. {ECO:0000305}.
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EMBL; M34052; AAA42142.1; -; mRNA.
EMBL; M59211; AAA41819.1; -; mRNA.
EMBL; M59313; AAA41820.1; ALT_SEQ; mRNA.
EMBL; X62839; CAA44643.1; -; mRNA.
EMBL; M84203; AAA42143.1; -; mRNA.
PIR; A39402; A39402.
PIR; B45292; B45292.
PIR; S22703; S22703.
RefSeq; NP_631962.1; NM_139216.1. [P22462-3]
RefSeq; NP_631963.1; NM_139217.1. [P22462-1]
RefSeq; XP_006241389.1; XM_006241327.3. [P22462-1]
RefSeq; XP_017450149.1; XM_017594660.1. [P22462-1]
RefSeq; XP_017450150.1; XM_017594661.1. [P22462-2]
RefSeq; XP_017450151.1; XM_017594662.1. [P22462-4]
RefSeq; XP_017450152.1; XM_017594663.1. [P22462-3]
UniGene; Rn.9733; -.
ProteinModelPortal; P22462; -.
BioGrid; 251521; 1.
STRING; 10116.ENSRNOP00000005773; -.
GuidetoPHARMACOLOGY; 549; -.
PhosphoSitePlus; P22462; -.
PaxDb; P22462; -.
PRIDE; P22462; -.
Ensembl; ENSRNOT00000005690; ENSRNOP00000005690; ENSRNOG00000004077. [P22462-3]
Ensembl; ENSRNOT00000005773; ENSRNOP00000005773; ENSRNOG00000004077. [P22462-1]
GeneID; 246153; -.
KEGG; rno:246153; -.
UCSC; RGD:628829; rat. [P22462-1]
CTD; 3747; -.
RGD; 628829; Kcnc2.
eggNOG; KOG3713; Eukaryota.
eggNOG; COG1226; LUCA.
GeneTree; ENSGT00760000118846; -.
HOGENOM; HOG000231012; -.
HOVERGEN; HBG105862; -.
InParanoid; P22462; -.
KO; K04888; -.
OMA; DLNMACN; -.
OrthoDB; EOG091G0EJL; -.
PhylomeDB; P22462; -.
TreeFam; TF352511; -.
Reactome; R-RNO-1296072; Voltage gated Potassium channels.
Reactome; R-RNO-381676; Glucagon-like Peptide-1 (GLP1) regulates insulin secretion.
PRO; PR:P22462; -.
Proteomes; UP000002494; Chromosome 7.
Bgee; ENSRNOG00000004077; -.
Genevisible; P22462; RN.
GO; GO:0016324; C:apical plasma membrane; IDA:UniProtKB.
GO; GO:0030673; C:axolemma; IDA:RGD.
GO; GO:0030424; C:axon; IDA:UniProtKB.
GO; GO:0016323; C:basolateral plasma membrane; IDA:RGD.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-KW.
GO; GO:0030425; C:dendrite; IDA:RGD.
GO; GO:0005887; C:integral component of plasma membrane; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0043025; C:neuronal cell body; IDA:RGD.
GO; GO:0032809; C:neuronal cell body membrane; IDA:UniProtKB.
GO; GO:0043204; C:perikaryon; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0045211; C:postsynaptic membrane; ISS:UniProtKB.
GO; GO:0042734; C:presynaptic membrane; ISS:UniProtKB.
GO; GO:0045202; C:synapse; IDA:UniProtKB.
GO; GO:0043195; C:terminal bouton; IDA:RGD.
GO; GO:0031982; C:vesicle; IDA:RGD.
GO; GO:0008076; C:voltage-gated potassium channel complex; IDA:UniProtKB.
GO; GO:0005251; F:delayed rectifier potassium channel activity; IDA:UniProtKB.
GO; GO:0044325; F:ion channel binding; IPI:UniProtKB.
GO; GO:0005249; F:voltage-gated potassium channel activity; IDA:UniProtKB.
GO; GO:0071242; P:cellular response to ammonium ion; IEP:RGD.
GO; GO:0071732; P:cellular response to nitric oxide; IDA:UniProtKB.
GO; GO:0097237; P:cellular response to toxic substance; IMP:RGD.
GO; GO:0021759; P:globus pallidus development; IEP:RGD.
GO; GO:0034220; P:ion transmembrane transport; IDA:RGD.
GO; GO:0038060; P:nitric oxide-cGMP-mediated signaling pathway; IDA:UniProtKB.
GO; GO:1901381; P:positive regulation of potassium ion transmembrane transport; IDA:RGD.
GO; GO:1903818; P:positive regulation of voltage-gated potassium channel activity; IDA:RGD.
GO; GO:0071805; P:potassium ion transmembrane transport; IDA:UniProtKB.
GO; GO:0051291; P:protein heterooligomerization; IDA:UniProtKB.
GO; GO:0051260; P:protein homooligomerization; IDA:UniProtKB.
GO; GO:0014075; P:response to amine; IEP:RGD.
GO; GO:0045471; P:response to ethanol; IEP:RGD.
GO; GO:0009642; P:response to light intensity; IEP:RGD.
GO; GO:0032026; P:response to magnesium ion; IEP:RGD.
GO; GO:1990089; P:response to nerve growth factor; IEP:RGD.
GO; GO:0014070; P:response to organic cyclic compound; IEP:RGD.
GO; GO:0009636; P:response to toxic substance; IEP:RGD.
Gene3D; 1.20.120.350; -; 1.
InterPro; IPR000210; BTB/POZ_dom.
InterPro; IPR005821; Ion_trans_dom.
InterPro; IPR003968; K_chnl_volt-dep_Kv.
InterPro; IPR003974; K_chnl_volt-dep_Kv3.
InterPro; IPR011333; SKP1/BTB/POZ_sf.
InterPro; IPR003131; T1-type_BTB.
InterPro; IPR028325; VG_K_chnl.
InterPro; IPR027359; Volt_channel_dom_sf.
PANTHER; PTHR11537; PTHR11537; 1.
Pfam; PF02214; BTB_2; 1.
Pfam; PF00520; Ion_trans; 1.
PRINTS; PR00169; KCHANNEL.
PRINTS; PR01491; KVCHANNEL.
PRINTS; PR01498; SHAWCHANNEL.
SMART; SM00225; BTB; 1.
SUPFAM; SSF54695; SSF54695; 2.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Complete proteome; Glycoprotein; Ion channel; Ion transport; Membrane;
Phosphoprotein; Postsynaptic cell membrane; Potassium;
Potassium channel; Potassium transport; Reference proteome; Synapse;
Synaptosome; Transmembrane; Transmembrane helix; Transport;
Voltage-gated channel.
CHAIN 1 638 Potassium voltage-gated channel subfamily
C member 2.
/FTId=PRO_0000054054.
TOPO_DOM 1 229 Cytoplasmic. {ECO:0000255}.
TRANSMEM 230 248 Helical; Name=Segment S1. {ECO:0000255}.
TRANSMEM 284 303 Helical; Name=Segment S2. {ECO:0000255}.
TOPO_DOM 304 314 Cytoplasmic. {ECO:0000255}.
TRANSMEM 315 337 Helical; Name=Segment S3. {ECO:0000255}.
TRANSMEM 346 368 Helical; Voltage-sensor; Name=Segment S4.
{ECO:0000255}.
TOPO_DOM 369 381 Cytoplasmic. {ECO:0000255}.
TRANSMEM 382 401 Helical; Name=Segment S5. {ECO:0000255}.
TRANSMEM 451 473 Helical; Name=Segment S6. {ECO:0000255}.
TOPO_DOM 474 638 Cytoplasmic. {ECO:0000255}.
MOTIF 437 442 Selectivity filter. {ECO:0000250}.
COMPBIAS 56 99 Gly/Pro-rich (insert).
MOD_RES 564 564 Phosphoserine; by PKA. {ECO:0000255}.
MOD_RES 600 600 Phosphoserine.
{ECO:0000250|UniProtKB:Q14B80}.
CARBOHYD 259 259 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
CARBOHYD 266 266 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
VAR_SEQ 594 638 GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPI
PSIL -> ASTLEPMESTSQTKGDTRPEAHWNCAHLLNFGC
PTGSSFPTL (in isoform 2).
{ECO:0000303|PubMed:1879548}.
/FTId=VSP_001018.
VAR_SEQ 594 638 GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPI
PSIL -> DNCKDVVITGYTQAEARSLT (in isoform
3). {ECO:0000303|PubMed:2367536}.
/FTId=VSP_001019.
VAR_SEQ 594 638 GYEKSRSLNNIAGLAGNALRLSPVTSPYNSPCPLRRSRSPI
PSIL -> VLYRIYHGFLPAENGTLRFSHSKDCTGNFCY
(in isoform 4).
{ECO:0000303|PubMed:1378392}.
/FTId=VSP_001020.
MUTAGEN 563 563 S->A: Does not abolish channel activity
inhibition in presence of nitric oxide
(NO); when associated with A-564. Absence
of channel activity inhibition in
presence of cAMP; when associated with A-
564. {ECO:0000269|PubMed:11281123,
ECO:0000269|PubMed:7643197}.
MUTAGEN 564 564 S->A: Does not abolish channel activity
inhibition in presence of nitric oxide
(NO); when associated with A-564. Absence
of channel activity inhibition in
presence of cAMP; when associated with A-
563. {ECO:0000269|PubMed:11281123,
ECO:0000269|PubMed:7643197}.
CONFLICT 2 2 G -> S (in Ref. 4; CAA44643).
{ECO:0000305}.
SEQUENCE 638 AA; 70191 MW; 25C102B4CCE53BF4 CRC64;
MGKIENNERV ILNVGGTRHE TYRSTLKTLP GTRLALLASS EPQGDCLTAA GDKLQPLPPP
LSPPPRPPPL SPVPSGCFEG GAGNCSSHGG NGSDHPGGGR EFFFDRHPGV FAYVLNYYRT
GKLHCPADVC GPLFEEELAF WGIDETDVEP CCWMTYRQHR DAEEALDIFE TPDLIGGDPG
DDEDLGGKRL GIEDAAGLGG PDGKSGRWRK LQPRMWALFE DPYSSRAARF IAFASLFFIL
VSITTFCLET HEAFNIVKNK TEPVINGTSA VLQYEIETDP ALTYVEGVCV VWFTFEFLVR
IVFSPNKLEF IKNLLNIIDF VAILPFYLEV GLSGLSSKAA KDVLGFLRVV RFVRILRIFK
LTRHFVGLRV LGHTLRASTN EFLLLIIFLA LGVLIFATMI YYAERVGAQP NDPSASEHTQ
FKNIPIGFWW AVVTMTTLGY GDMYPQTWSG MLVGALCALA GVLTIAMPVP VIVNNFGMYY
SLAMAKQKLP RKRKKHIPPA PLASSPTFCK TELNMACNST QSDTCLGKEN RLLEHNRSVL
SGDDSTGSEP PLSPPERLPI RRSSTRDKNR RGETCFLLTT GDYTCASDGG IRKGYEKSRS
LNNIAGLAGN ALRLSPVTSP YNSPCPLRRS RSPIPSIL


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